ID   SPZ10_ARATH             Reviewed;         385 AA.
AC   Q9SIR9; Q5PP54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Serpin-Z10;
DE   AltName: Full=ArathZ10;
GN   OrderedLocusNames=At2g25240; ORFNames=T22F11.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-385.
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18060440; DOI=10.1007/s10142-007-0059-2;
RA   Roberts T.H., Hejgaard J.;
RT   "Serpins in plants and green algae.";
RL   Funct. Integr. Genomics 8:1-27(2008).
CC   -!- FUNCTION: Probable serine protease inhibitor. {ECO:0000250}.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV74237.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC007070; AAD23667.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07675.1; -; Genomic_DNA.
DR   EMBL; BT020243; AAV74237.1; ALT_INIT; mRNA.
DR   EMBL; BT022062; AAY25474.1; -; mRNA.
DR   PIR; A84646; A84646.
DR   RefSeq; NP_180096.3; NM_128081.4.
DR   AlphaFoldDB; Q9SIR9; -.
DR   SMR; Q9SIR9; -.
DR   STRING; 3702.AT2G25240.1; -.
DR   PaxDb; Q9SIR9; -.
DR   PRIDE; Q9SIR9; -.
DR   ProteomicsDB; 226912; -.
DR   EnsemblPlants; AT2G25240.1; AT2G25240.1; AT2G25240.
DR   GeneID; 817062; -.
DR   Gramene; AT2G25240.1; AT2G25240.1; AT2G25240.
DR   KEGG; ath:AT2G25240; -.
DR   Araport; AT2G25240; -.
DR   TAIR; locus:2059585; AT2G25240.
DR   eggNOG; KOG2392; Eukaryota.
DR   HOGENOM; CLU_023330_4_0_1; -.
DR   InParanoid; Q9SIR9; -.
DR   OMA; NCIFFCG; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; Q9SIR9; -.
DR   PRO; PR:Q9SIR9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIR9; baseline and differential.
DR   Genevisible; Q9SIR9; AT.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   2: Evidence at transcript level;
KW   Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..385
FT                   /note="Serpin-Z10"
FT                   /id="PRO_0000334551"
FT   REGION          333..357
FT                   /note="RCL"
FT   SITE            347..348
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   385 AA;  42724 MW;  62438FA72316E01E CRC64;
     MELGKSIENH NDVVVRLTKH VIATVANGSN LVFSPISINV LLSLIAAGSC SVTKEQILSF
     LMLPSTDHLN LVLAQIIDGG TEKSDLRLSI ANGVWIDKFF SLKLSFKDLL ENSYKATCSQ
     VDFASKPSEV IDEVNTWAEV HTNGLIKQIL SRDSIDTIRS STLVLANAVY FKGAWSSKFD
     ANMTKKNDFH LLDGTSVKVP FMTNYEDQYL RSYDGFKVLR LPYIEDQRQF SMYIYLPNDK
     EGLAPLLEKI GSEPSFFDNH IPLHCISVGA FRIPKFKFSF EFNASEVLKD MGLTSPFNNG
     GGLTEMVDSP SNGDDLYVSS ILHKACIEVD EEGTEAAAVS VGVVSCTSFR RNPDFVADRP
     FLFTVREDKS GVILFMGQVL DPSKH